Structure of PDB 5evb Chain A

Receptor sequence
>5evbA (length=266) Species: 40324 (Stenotrophomonas maltophilia) [Search protein sequence]
EVPLPQLRAYTVDASWLQPMAPLQIADHTWQIGTEDLTALLVQTPDGAVL
LDGGMPQMASHLLDNMKARGVTPRDLRLILLSHAHADHAGPVAELKRRTG
AKVAANAESAVLLARGGSDDLHFGDGITYPPANADRIVMDGEVITVGGIV
FTAHFMAGHTPGSTAWTWTDTRNGKPVRIAYADSLSAPGYQLQGNPRYPH
LIEDYRRSFATVRALPCDVLLTPHPGASNWDYAAGARAGAKALTCKAYAD
AAEQKFDGQLAKETAG
3D structure
PDB5evb Cross-class metallo-beta-lactamase inhibition by bisthiazolidines reveals multiple binding modes.
ChainA
Resolution1.841 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H116 H118 D120 H121 H196 Y229 H263
Catalytic site (residue number reindexed from 1) H83 H85 D87 H88 H159 Y190 H224
Enzyme Commision number 3.5.2.6: beta-lactamase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN A H116 H118 H196 H83 H85 H159
BS02 ZN A D120 H121 H263 D87 H88 H224
BS03 3R9 A H118 D120 F156 I162 H196 P227 H85 D87 F123 I127 H159 P188 MOAD: Ki=10uM
PDBbind-CN: -logKd/Ki=5.00,Ki=10uM
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0008800 beta-lactamase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0017001 antibiotic catabolic process
GO:0030655 beta-lactam antibiotic catabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0042597 periplasmic space

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Cellular Component
External links
PDB RCSB:5evb, PDBe:5evb, PDBj:5evb
PDBsum5evb
PubMed27303030
UniProtP52700|BLA1_STEMA Metallo-beta-lactamase L1 type 3

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